6HE3
Pseudomonas aeruginosa Seryl-tRNA Synthetase in Complex with 5'-O-(N-(L-seryl)-sulfamoyl)cytidine
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000166 | molecular_function | nucleotide binding |
A | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
A | 0004828 | molecular_function | serine-tRNA ligase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0006412 | biological_process | translation |
A | 0006418 | biological_process | tRNA aminoacylation for protein translation |
A | 0006434 | biological_process | seryl-tRNA aminoacylation |
A | 0016260 | biological_process | selenocysteine biosynthetic process |
B | 0000166 | molecular_function | nucleotide binding |
B | 0004812 | molecular_function | aminoacyl-tRNA ligase activity |
B | 0004828 | molecular_function | serine-tRNA ligase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0006412 | biological_process | translation |
B | 0006418 | biological_process | tRNA aminoacylation for protein translation |
B | 0006434 | biological_process | seryl-tRNA aminoacylation |
B | 0016260 | biological_process | selenocysteine biosynthetic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | binding site for residue EDO A 501 |
Chain | Residue |
A | GLU316 |
A | ASN401 |
A | TYR402 |
A | HOH630 |
A | HOH709 |
site_id | AC2 |
Number of Residues | 10 |
Details | binding site for residue EDO A 502 |
Chain | Residue |
A | PHE283 |
A | ASP284 |
A | GLY392 |
A | HOH616 |
A | HOH656 |
B | TYR194 |
A | MET165 |
A | HIS173 |
A | MET277 |
A | GLN282 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue EDO A 503 |
Chain | Residue |
A | GLN209 |
A | PRO232 |
A | THR233 |
A | GLU235 |
A | FZQ504 |
A | HOH703 |
site_id | AC4 |
Number of Residues | 21 |
Details | binding site for residue FZQ A 504 |
Chain | Residue |
A | THR233 |
A | GLU235 |
A | ARG264 |
A | GLU266 |
A | ILE278 |
A | GLN280 |
A | PHE283 |
A | GLU287 |
A | GLU351 |
A | ILE352 |
A | SER353 |
A | SER354 |
A | ASN385 |
A | SER387 |
A | ALA390 |
A | ARG393 |
A | EDO503 |
A | NA505 |
A | HOH644 |
A | HOH679 |
A | HOH687 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue NA A 505 |
Chain | Residue |
A | GLU351 |
A | SER354 |
A | FZQ504 |
A | HOH660 |
A | HOH757 |
A | HOH769 |
site_id | AC6 |
Number of Residues | 4 |
Details | binding site for residue EDO B 501 |
Chain | Residue |
B | GLU316 |
B | ASN401 |
B | TYR402 |
B | HOH611 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue EDO B 502 |
Chain | Residue |
A | TRP126 |
A | GLY127 |
B | GLU122 |
B | ARG125 |
site_id | AC8 |
Number of Residues | 10 |
Details | binding site for residue EDO B 503 |
Chain | Residue |
A | TYR194 |
B | MET165 |
B | HIS173 |
B | MET277 |
B | GLN282 |
B | PHE283 |
B | ASP284 |
B | GLY392 |
B | HOH605 |
B | HOH646 |
site_id | AC9 |
Number of Residues | 21 |
Details | binding site for residue FZQ B 504 |
Chain | Residue |
B | THR233 |
B | GLU235 |
B | ARG264 |
B | GLU266 |
B | ILE278 |
B | GLN280 |
B | PHE283 |
B | LYS285 |
B | GLU287 |
B | GLU351 |
B | ILE352 |
B | SER353 |
B | SER354 |
B | ASN385 |
B | SER387 |
B | ALA390 |
B | ARG393 |
B | NA505 |
B | HOH648 |
B | HOH663 |
B | HOH668 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue NA B 505 |
Chain | Residue |
B | GLU351 |
B | SER354 |
B | FZQ504 |
B | HOH677 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00176 |
Chain | Residue | Details |
A | THR233 | |
B | SER387 | |
A | ARG264 | |
A | GLU287 | |
A | GLU351 | |
A | SER387 | |
B | THR233 | |
B | ARG264 | |
B | GLU287 | |
B | GLU351 |